NDLI: Characterization of anti-peptide antibodies for the localization of D2 dopamine receptors in rat striatum.

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Characterization of anti-peptide antibodies for the localization of D2 dopamine receptors in rat striatum.

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Characterization of anti-peptide antibodies for the localization of D2 dopamine receptors in rat striatum.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mcvittie, L. D. Ariano, M. A. Sibley, D. R.
Description	Author Affiliation: McVittie LD ( Experimental Therapeutics Branch, National Institutes of Neurological Disorders and Stroke, Bethesda, MD 20892.);
Abstract	Seven different peptides of 14-23 residues in length based on the predicted amino acid sequence of the cloned rat D2 receptor cDNA were used as immunogens to develop antibodies in rabbits. Two of these peptides were derived from the amino terminus and four were from the third cytoplasmic loop, including one to the splice variant insertion sequence and one to the carboxyl terminus of the receptor protein. These peptides were conjugated to bovine thyroglobulin prior to rabbit immunization. Antibody production was monitored by a solid-phase ELISA. With the exception of the carboxyl-terminal peptide, all of the peptide immunogens produced antiserum of high titer ranging from 1:10(4) to 1:10(6) on ELISA. Specificity of the reaction was demonstrated by the absence of a response in the preimmune serum and by the absence of cross-reactivity between the various antisera and the nonimmunization peptides. Moreover, preincubation of the antiserum with the immunization peptide, but not other peptides, blocked the subsequent ELISA reactions. Some of the antisera were additionally characterized by immunodot assays using solubilized rat striatal membranes blotted onto nitrocellulose. Positive reactions with antiserum dilutions of 1:500 were observed that were dependent on the presence and concentration of membrane protein and were not observed using preimmune serum. Additionally, immunofluorescent staining by the D2 receptor antiserum was observed on cells that had been transfected with the D2 receptor cDNA but not on untransfected cells. Immunoprecipitation of the photoaffinity-labelled and solubilized D2 receptor also suggested that the antisera were able to directly recognize the native receptor protein. Immunohistochemical localization of the D2 receptor in slices of fresh frozen and perfusion-fixed rat brain was performed using these antisera. Within the striatum, about 50% of the medium-sized neurons were labeled as well as large, putatively cholinergic interneurons.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Antibodies Corpus Striatum Metabolism Receptors, Dopamine Amino Acid Sequence Animals Antigen-Antibody Complex Cell Line Cytology Enzyme-Linked Immunosorbent Assay Fluorescent Antibody Technique Immunohistochemistry Molecular Sequence Data Peptides Chemical Synthesis Genetics Receptors, Dopamine D2 Transfection Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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